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Encompasses the method of analytical ultracentrifugation to determine native mass, stoichiometry and shape of proteins and biomolecular complexes in solution; and the techniques of isothermal titration microcalorimetry (ITC) and microscale thermophoresis (MST) to measure the thermodynamics of protein-protein and protein-ligand interactions. The recent addition of surface plasmon resonance (SPR) spectroscopy to this capability has enabled the measurement of binding kinetics to complement thermodynamic analyses.